Host apoplastic cysteine protease activity is suppressed during the mutualistic association of Lolium perenne and Epichloë festucae

Bibliographische Detailangaben
Veröffentlicht in:	Journal of experimental botany. - 1985. - 72(2021), 9 vom: 13. Apr., Seite 3410-3426
1. Verfasser:	Passarge, Andrea (VerfasserIn)
Weitere Verfasser:	Demir, Fatih, Green, Kimberly, Depotter, Jasper R L, Scott, Barry, Huesgen, Pitter F, Doehlemann, Gunther, Misas Villamil, Johana C
Format:	Online-Aufsatz
Sprache:	English
Veröffentlicht:	2021
Zugriff auf das übergeordnete Werk:	Journal of experimental botany
Schlagworte:	Journal Article Research Support, Non-U.S. Gov't Apoplast cystatin endophyte papain-like cysteine proteases ryegrass Plant Proteins Cysteine Proteases EC 3.4.-

Beschreibung
Zusammenfassung:	© The Author(s) 2021. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com. Plants secrete various defence-related proteins into the apoplast, including proteases. Papain-like cysteine proteases (PLCPs) are central components of the plant immune system. To overcome plant immunity and successfully colonize their hosts, several plant pathogens secrete effector proteins inhibiting plant PLCPs. We hypothesized that not only pathogens, but also mutualistic microorganisms interfere with PLCP-meditated plant defences to maintain endophytic colonization with their hosts. Epichloë festucae forms mutualistic associations with cool season grasses and produces a range of secondary metabolites that protect the host against herbivores. In this study, we performed a genome-wide identification of Lolium perenne PLCPs, analysed their evolutionary relationship, and classified them into nine PLCP subfamilies. Using activity-based protein profiling, we identified four active PLCPs in the apoplast of L. perenne leaves that are inhibited during endophyte interactions. We characterized the L. perenne cystatin LpCys1 for its inhibitory capacity against ryegrass PLCPs. LpCys1 abundance is not altered during the mutualistic interaction and it mainly inhibits LpCP2. However, since the activity of other L. perenne PLCPs is not sensitive to LpCys1, we propose that additional inhibitors, likely of fungal origin, are involved in the suppression of apoplastic PLCPs during E. festucae infection
Beschreibung:	Date Completed 21.05.2021 Date Revised 31.05.2022 published: Print Citation Status MEDLINE
ISSN:	1460-2431
DOI:	10.1093/jxb/erab088